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    KIRREL1 kirre like nephrin family adhesion molecule 1 [ Homo sapiens (human) ]

    Gene ID: 55243, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    KIRREL promotes the proliferation of gastric cancer cells and angiogenesis through the PI3K/AKT/mTOR pathway.

    KIRREL promotes the proliferation of gastric cancer cells and angiogenesis through the PI3K/AKT/mTOR pathway.
    Wang T, Chen S, Wang Z, Li S, Fei X, Wang T, Zhang M., Free PMC Article

    01/30/2024
    Transmembrane protein KIRREL1 regulates Hippo signaling via a feedback loop and represents a therapeutic target in YAP/TAZ-active cancers.

    Transmembrane protein KIRREL1 regulates Hippo signaling via a feedback loop and represents a therapeutic target in YAP/TAZ-active cancers.
    Gu Y, Wang Y, Sha Z, He C, Zhu Y, Li J, Yu A, Zhong Z, Wang X, Sun Y, Lan F, Yu FX.

    09/24/2022
    Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo signaling recruiting SAV1 to cell-cell contact sites.

    Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo signaling recruiting SAV1 to cell-cell contact sites.
    Paul A, Annunziato S, Lu B, Sun T, Evrova O, Planas-Paz L, Orsini V, Terracciano LM, Charlat O, Loureiro ZY, Ji L, Zamponi R, Sigoillot F, Lei H, Lindeman A, Russ C, Reece-Hoyes JS, Nicholson TB, Tchorz JS, Cong F., Free PMC Article

    03/5/2022
    Overexpression of kin of IRRE-Like protein 1 (KIRREL) as a prognostic biomarker for breast cancer.

    Overexpression of kin of IRRE-Like protein 1 (KIRREL) as a prognostic biomarker for breast cancer.
    Chen K, Zhao R, Yao G, Liu Z, Shi R, Geng J.

    04/3/2021
    Mutations in KIRREL1, a slit diaphragm component, cause steroid-resistant nephrotic syndrome.

    Mutations in KIRREL1, a slit diaphragm component, cause steroid-resistant nephrotic syndrome.
    Solanki AK, Widmeier E, Arif E, Sharma S, Daga A, Srivastava P, Kwon SH, Hugo H, Nakayama M, Mann N, Majmundar AJ, Tan W, Gee HY, Sadowski CE, Rinat C, Becker-Cohen R, Bergmann C, Rosen S, Somers M, Shril S, Huber TB, Mane S, Hildebrandt F, Nihalani D., Free PMC Article

    10/24/2020
    Analysis of interaction surfaces between NEPH1 and MYO1c led to the identification of a critical residue in Neph1 involved in binding to Myo1c. Indeed, a point mutant from this site abolished interaction between Neph1 and Myo1c.

    Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1.
    Arif E, Sharma P, Solanki A, Mallik L, Rathore YS, Twal WO, Nath SK, Gandhi D, Holzman LB, Ostap EM, Ashish, Nihalani D., Free PMC Article

    05/27/2017
    maintaining high levels of Neph1 at the membrane using a podocyte cell line overexpressing chimeric Neph1 increased the ability of podocytes to resist PAN-induced injury and PAN-induced albumin leakage

    Slit diaphragm protein Neph1 and its signaling: a novel therapeutic target for protection of podocytes against glomerular injury.
    Arif E, Rathore YS, Kumari B, Ashish F, Wong HN, Holzman LB, Nihalani D., Free PMC Article

    05/31/2014
    Neph1-CD adopts a global shape in solution, and its interaction with ZO-1 involves multiple sites.

    Solution structure analysis of cytoplasmic domain of podocyte protein Neph1 using small/wide angle x-ray scattering (SWAXS).
    Mallik L, Arif E, Sharma P, Rathore YS, Wong HN, Holzman LB, Ashish, Nihalani D., Free PMC Article

    06/16/2012
    Localization of Neph1 to the podocyte cell membrane is altered in the presence of mutant Myo1c, and is actin dependent. Knockdown of Myo1c inhibits Neph1 membrane localization. Neph1 is critical for the maintenance of glomerular function.

    Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane.
    Arif E, Wagner MC, Johnstone DB, Wong HN, George B, Pruthi PA, Lazzara MJ, Nihalani D., Free PMC Article

    07/2/2011
    tyrosine phosphorylation of Neph1 mediated by Fyn results in significantly increased Neph1 and ZO-1 binding, suggesting a critical role for Neph1 tyrosine phosphorylation in reorganizing the Neph1-ZO-1 complex.

    Ischemic injury to kidney induces glomerular podocyte effacement and dissociation of slit diaphragm proteins Neph1 and ZO-1.
    Wagner MC, Rhodes G, Wang E, Pruthi V, Arif E, Saleem MA, Wean SE, Garg P, Verma R, Holzman LB, Gattone V, Molitoris BA, Nihalani D., Free PMC Article

    01/21/2010
    common variants in LRRC7, KIRREL, NPHS2 and ACTN4 do not appeear to contribute to susceptibility to diabetic nephropathy in Finnish patients with type 1 diabetes

    Association analysis of podocyte slit diaphragm genes as candidates for diabetic nephropathy.
    Ihalmo P, Wessman M, Kaunisto MA, Kilpikari R, Parkkonen M, Forsblom C, Holthöfer H, Groop PH, FinnDiane Study Group, Ihalmo P, Wessman M, Kaunisto MA, Kilpikari R, Parkkonen M, Forsblom C, Holthöfer H, Groop PH, FinnDiane Study Group.

    01/21/2010
    Neph1-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity

    Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity.
    Hartleben B, Schweizer H, Lübben P, Bartram MP, Möller CC, Herr R, Wei C, Neumann-Haefelin E, Schermer B, Zentgraf H, Kerjaschki D, Reiser J, Walz G, Benzing T, Huber TB., Free PMC Article

    01/21/2010
    Neph1 but not nephrin specifically binds to adaptor protein Grb2 and tyrosine kinase Csk in a phosphorylation-dependent manner.

    Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2.
    Harita Y, Kurihara H, Kosako H, Tezuka T, Sekine T, Igarashi T, Hattori S., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    Genotype-phenotype correlations in non-Finnish congenital nephrotic syndrome.
    Machuca E, Benoit G, Nevo F, Tête MJ, Gribouval O, Pawtowski A, Brandström P, Loirat C, Niaudet P, Gubler MC, Antignac C.

    Association analysis of podocyte slit diaphragm genes as candidates for diabetic nephropathy.
    Ihalmo P, Wessman M, Kaunisto MA, Kilpikari R, Parkkonen M, Forsblom C, Holthöfer H, Groop PH, FinnDiane Study Group, Ihalmo P, Wessman M, Kaunisto MA, Kilpikari R, Parkkonen M, Forsblom C, Holthöfer H, Groop PH, FinnDiane Study Group.

    03/13/2008
    A striking finding in this study is the lack of contribution of NEPH1, NPHS1, and NPHS2 genes in 15 Asian families with steroid-resistant nephrotic syndrome.

    Genetics and clinical features of 15 Asian families with steroid-resistant nephrotic syndrome.
    Kitamura A, Tsukaguchi H, Iijima K, Araki J, Hattori M, Ikeda M, Honda M, Nozu K, Nakazato H, Yoshikawa N, Kagami S, Muramatsu M, Choi Y, Cheong HI, Doi T.

    01/21/2010
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